(data stored in ACNUC7421 zone)

SWISSPROT: B1VNG3_STRGG

ID   B1VNG3_STRGG            Unreviewed;       351 AA.
AC   B1VNG3;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   07-JUN-2017, entry version 72.
DE   RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA {ECO:0000256|HAMAP-Rule:MF_01820};
DE            EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_01820};
GN   Name=rsgA {ECO:0000256|HAMAP-Rule:MF_01820};
GN   OrderedLocusNames=SGR_157 {ECO:0000313|EMBL:BAG16986.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG16986.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG16986.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- FUNCTION: One of several proteins that assist in the late
CC       maturation steps of the functional core of the 30S ribosomal
CC       subunit. Helps release RbfA from mature subunits. May play a role
CC       in the assembly of ribosomal proteins into the subunit. Circularly
CC       permuted GTPase that catalyzes slow GTP hydrolysis, GTPase
CC       activity is stimulated by the 30S ribosomal subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_01820, ECO:0000256|SAAS:SAAS00828801}.
CC   -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC       rRNA. {ECO:0000256|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00828796}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00820346}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC       RsgA subfamily. {ECO:0000256|SAAS:SAAS00720088}.
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DR   EMBL; AP009493; BAG16986.1; -; Genomic_DNA.
DR   ProteinModelPortal; B1VNG3; -.
DR   STRING; 455632.SGR_157; -.
DR   EnsemblBacteria; BAG16986; BAG16986; SGR_157.
DR   KEGG; sgr:SGR_157; -.
DR   eggNOG; ENOG4105E06; Bacteria.
DR   eggNOG; COG1162; LUCA.
DR   HOGENOM; HOG000006956; -.
DR   KO; K06949; -.
DR   OMA; MQRELEY; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-HAMAP.
DR   CDD; cd01854; YjeQ_EngC; 1.
DR   HAMAP; MF_01820; GTPase_RsgA; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA.
DR   InterPro; IPR010914; RsgA_GTPase_dom.
DR   PANTHER; PTHR32120; PTHR32120; 1.
DR   Pfam; PF03193; RsgA_GTPase; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00157; TIGR00157; 1.
DR   PROSITE; PS50936; ENGC_GTPASE; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1VNG3.
DR   SWISS-2DPAGE; B1VNG3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00820338};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00698892};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720101};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720208};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00698882};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001685};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720213};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720223};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720235};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01820, ECO:0000256|SAAS:SAAS00720226}.
FT   DOMAIN       97    252       CP-type G (guanine nucleotide-binding).
FT                                {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN      105    250       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     144    147       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     194    202       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       275    275       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       280    280       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       282    282       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       288    288       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   351 AA;  37087 MW;  E9F7A3A953A819D7 CRC64;
     MADYGWDAER ERSFGPSRDE GLVPGRAVRA ERGLCDVVAE TGPVRAMVLP SSGTGDRLTP
     CTGDWVSVRP AGPATSATVV EVLERRTAVV RSTSSRTSHA QVLASNVDTV AVAVSLADPL
     KLGRIERTLA LAWESGATPV IVLTKADRST DPASAASEVA EAAPGVEVLV TSATTGEGLD
     ILTAVLSGTV VLLGPSGAGK STLGNRLLGE DLLATGEVRG SDGKGRHTTA WRELVPLPHG
     GVLLDTPGLR GVGLHDADDG LEHTFAEITE LARDCRFADC AHTTEPGCAV LAAVEDGRLT
     QRRLDSYHRL QRENTYAAAR TDARLRAELE RPMKQISRQV RALKQSPHFK A
//

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